It is generally believed that all biological functions can be interpreted on a molecular level and that there exists a structure-function relationship. Optical rotatory dispersion (ORD) and circular dichroism (CD) have now been widely used in studying the conformation of biopolymers in solution. We have recently developed a method of analysis, which allows us to determine the percentages of helix and beta-form in a protein molecule. One of our objectives will be to study the relative change in helix and beta-form that accompanies denaturation or partial hydrolysis (enzymatic). Proteins of known structure will be studied first. Biological activities at each stage of denaturation will be correlated with the secondary structure of the protein molecule. Second, the effect of detergents on protein conformation will be systematically studied with the use of homogeneous (as distinguished from commercial mixtures) detergents specifically synthesized for this purpose. Our objective is to gain a better understanding of the hydrophobic interaction of these detergents with respect to protein conformation. BIBLIOGRAPHIC REFERENCES: Yang, J.T., Chen, G.C. and Jorgensons, B. (1976) Optical Rotatory Dispersion and Circular Dichroism of Proteins. In Handbood of Biochemistry and Molecular Biology, 3rd Ed., G.D. Fasman, Ed., Vol. IA. CRC Press, Inc., Cleveland, Ohio, in press.